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Phosphoenolpyruvate-dependent phosphotransferase system. ¹H NMR studies on chemically modified HPr proteins

Kalbitzer, Hans Robert and Muss, H. P. and Engelmann, R. and Kiltz, H. H. and Stüber, K. and Hengstenberg, W. (1985) Phosphoenolpyruvate-dependent phosphotransferase system. ¹H NMR studies on chemically modified HPr proteins. Biochemistry 24 (17), pp. 4562-4569.

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Abstract

The low-pK tyrosyl residue present in the heat-stable proteins (HPr) of all Gram-positive bacteria studied until now has been labeled by tetranitromethane in the HPr of Bacillus subtilis and Streptococcus faecalis. The nitrotyrosyl derivatives obtained are fully active in the complementation assay. The labeled tyrosyl residues could be identified as Tyr-37 in both proteins. Reinvestigation of the ...

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Item Type:Article
Date:1985
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
3933558PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Bacillus subtilis/enzymologyMESH
Bacterial ProteinsMESH
Binding SitesMESH
Chromatography, High Pressure LiquidMESH
Enterococcus faecalis/enzymologyMESH
Hydrogen-Ion ConcentrationMESH
KineticsMESH
Magnetic Resonance Spectroscopy/methodsMESH
Methane/analogs & derivativesMESH
Peptide Fragments/analysisMESH
Phosphoenolpyruvate Sugar Phosphotransferase System/metabolismMESH
Species SpecificityMESH
Staphylococcus aureus/enzymologyMESH
Tetranitromethane/pharmacologyMESH
TrypsinMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:02 Sep 2010 06:22
Last Modified:02 Sep 2010 06:22
Item ID:16438
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